DB code: S00157
CATH domain | 2.60.130.10 : Protocatechuate 3,4-Dioxygenase, subunit A | Catalytic domain |
---|---|---|
E.C. | 1.13.11.1 | |
CSA | ||
M-CSA | ||
MACiE |
CATH domain | Related DB codes (homologues) |
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Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P07773 |
Catechol 1,2-dioxygenase
|
EC
1.13.11.1
1,2-CTD |
YP_046127.1
(Protein)
NC_005966.1 (DNA/RNA sequence) |
PF00775
(Dioxygenase_C)
PF04444 (Dioxygenase_N) [Graphical View] |
KEGG enzyme name |
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catechol 1,2-dioxygenase
catechol-oxygen 1,2-oxidoreductase 1,2-pyrocatechase catechase catechol 1,2-oxygenase catechol dioxygenase pyrocatechase pyrocatechol 1,2-dioxygenase CD I CD II |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P07773 | CATA_ACIAD | Catechol + O(2) = cis,cis-muconate. | Homodimer. | Binds 1 Fe(3+) ion per subunit. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00361 | gamma-Hexachlorocyclohexane degradation | |
MAP00362 | Benzoate degradation via hydroxylation | |
MAP00364 | Fluorobenzoate degradation | |
MAP00622 | Toluene and xylene degradation | |
MAP00627 | 1,4-Dichlorobenzene degradation | |
MAP00629 | Carbazole degradation |
Compound table | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | |||||||
KEGG-id | C00023 | C00090 | C00007 | C02480 | ||||||
E.C. | ||||||||||
Compound | Iron | Catechol | O2 | cis,cis-Muconate | ||||||
Type | heavy metal | aromatic ring (only carbon atom) | others | carboxyl group | ||||||
ChEBI |
18248 82664 18248 82664 |
18135 18135 |
15379 26689 27140 15379 26689 27140 |
16508 16508 |
||||||
PubChem |
23925 23925 |
289 289 |
977 977 |
5280518 5280518 |
||||||
1dlmA | Bound:_FE | Unbound | Unbound | Unbound | ||||||
1dlmB | Bound:_FE | Unbound | Unbound | Unbound | ||||||
1dlqA | Bound:_FE | Unbound | Unbound | Unbound | ||||||
1dlqB | Bound:_FE | Unbound | Unbound | Unbound | ||||||
1dltA | Bound:_FE | Bound:CAQ | Unbound | Unbound | ||||||
1dltB | Bound:_FE | Bound:CAQ | Unbound | Unbound | ||||||
1dmhA | Bound:_FE | Analogue:MCT | Unbound | Unbound | ||||||
1dmhB | Bound:_FE | Analogue:MCT | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [14] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1dlmA | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dlmB | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dlqA | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dlqB | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dltA | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dltB | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dmhA | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) | ||||||||
1dmhB | TYR 200;ARG 221 | TYR 164;TYR 200;HIS 224;HIS 226(Fe binding) |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[2]
|
Fig.12, p.8471 | |
[4]
|
Fig.7 | |
[10]
|
Fig.3, Fig.4, p.95-96 | 6 |
[14]
|
Fig.6, p.436 | 1 |
[15]
|
p.3187-3189, Scheme 4 | |
[17]
|
Scheme 1, p.8291-8293 | 1 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 238971 |
Journal | J Biol Chem |
Year | 1975 |
Volume | 250 |
Pages | 4848-55 |
Authors | Fujiwara M, Golovleva LA, Saeki Y, Nozaki M, Hayaishi O |
Title |
Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6773944 |
Journal | J Biol Chem |
Year | 1980 |
Volume | 255 |
Pages | 8465-71 |
Authors | Saeki Y, Nozaki M, Senoh S |
Title | Cleavage of pyrogallol by non-heme iron-containing dioxygenases. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3015028 |
Journal | Arch Biochem Biophys |
Year | 1986 |
Volume | 248 |
Pages | 130-7 |
Authors | Pascal RA Jr, Huang DS |
Title | Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3365096 |
Journal | Arch Microbiol |
Year | 1988 |
Volume | 149 |
Pages | 188-97 |
Authors | Engesser KH, Cain RB, Knackmuss HJ |
Title | Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2394680 |
Journal | J Bacteriol |
Year | 1990 |
Volume | 172 |
Pages | 5119-29 |
Authors | Schlomann M, Fischer P, Schmidt E, Knackmuss HJ |
Title |
Enzymatic formation, |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1649626 |
Journal | Biochemistry |
Year | 1991 |
Volume | 30 |
Pages | 7349-58 |
Authors | Broderick JB, O'Halloran TV |
Title |
Overproduction, |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8107120 |
Journal | J Mol Biol |
Year | 1994 |
Volume | 236 |
Pages | 377-8 |
Authors | Earhart CA, Hall MD, Michaud-Soret I, Que L Jr, Ohlendorf DH |
Title | Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9369233 |
Journal | FEBS Lett |
Year | 1997 |
Volume | 416 |
Pages | 61-4 |
Authors | Briganti F, Pessione E, Giunta C, Scozzafava A |
Title |
Purification, |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9677336 |
Journal | Biochem J |
Year | 1998 |
Volume | 333 |
Pages | 741-7 |
Authors | Strachan PD, Freer AA, Fewson CA |
Title | Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9799107 |
Journal | Eur J Biochem |
Year | 1998 |
Volume | 257 |
Pages | 92-100 |
Authors | Ridder L, Briganti F, Boersma MG, Boeren S, Vis EH, Scozzafava A, Veeger C, Rietjens IM |
Title | Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10515940 |
Journal | J Bacteriol |
Year | 1999 |
Volume | 181 |
Pages | 6478-87 |
Authors | D'Argenio DA, Vetting MW, Ohlendorf DH, Ornston LN |
Title |
Substitution, |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10438749 |
Journal | J Bacteriol |
Year | 1999 |
Volume | 181 |
Pages | 4812-7 |
Authors | Riegert U, Heiss G, Kuhm AE, Muller C, Contzen M, Knackmuss HJ, Stolz A |
Title |
Catalytic properties of the 3-chlorocatechol-oxidizing 2, |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11307956 |
Journal | J Protein Chem |
Year | 2000 |
Volume | 19 |
Pages | 709-16 |
Authors | Briganti F, Pessione E, Giunta C, Mazzoli R, Scozzafava A |
Title | Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens. |
Related PDB | |
Related UniProtKB | |
[14] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10801478 |
Journal | Structure Fold Des |
Year | 2000 |
Volume | 8 |
Pages | 429-40 |
Authors | Vetting MW, Ohlendorf DH |
Title | The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. |
Related PDB | 1dlm 1dlq 1dlt 1dmh |
Related UniProtKB | P07773 |
[15] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11399191 |
Journal | Inorg Chem |
Year | 2001 |
Volume | 40 |
Pages | 3181-90 |
Authors | Jo DH, Chiou YM, Que L Jr |
Title |
Models for extradiol cleaving catechol dioxygenases: syntheses, |
Related PDB | |
Related UniProtKB | |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12450835 |
Journal | Appl Environ Microbiol |
Year | 2002 |
Volume | 68 |
Pages | 6114-20 |
Authors | Haroune N, Combourieu B, Besse P, Sancelme M, Reemtsma T, Kloepfer A, Diab A, Knapp JS, Baumberg S, Delort AM |
Title | Benzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity. |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 14658880 |
Journal | Inorg Chem |
Year | 2003 |
Volume | 42 |
Pages | 8283-93 |
Authors | Velusamy M, Palaniandavar M, Gopalan RS, Kulkarni GU |
Title | Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases. |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-07-07 | 2009-03-19 |